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TitleThe free fatty acid-binding pocket is a conserved hallmark in pathogenic β-coronavirus spike proteins from SARS-CoV to Omicron.
Journal, issue, pagesSci Adv, Vol. 8, Issue 47, Page eadc9179, Year 2022
Publish dateNov 25, 2022
AuthorsChristine Toelzer / Kapil Gupta / Sathish K N Yadav / Lorna Hodgson / Maia Kavanagh Williamson / Dora Buzas / Ufuk Borucu / Kyle Powers / Richard Stenner / Kate Vasileiou / Frederic Garzoni / Daniel Fitzgerald / Christine Payré / Gunjan Gautam / Gérard Lambeau / Andrew D Davidson / Paul Verkade / Martin Frank / Imre Berger / Christiane Schaffitzel /
PubMed AbstractAs coronavirus disease 2019 (COVID-19) persists, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) emerge, accumulating spike (S) glycoprotein mutations. S ...As coronavirus disease 2019 (COVID-19) persists, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) emerge, accumulating spike (S) glycoprotein mutations. S receptor binding domain (RBD) comprises a free fatty acid (FFA)-binding pocket. FFA binding stabilizes a locked S conformation, interfering with virus infectivity. We provide evidence that the pocket is conserved in pathogenic β-coronaviruses (β-CoVs) infecting humans. SARS-CoV, MERS-CoV, SARS-CoV-2, and VOCs bind the essential FFA linoleic acid (LA), while binding is abolished by one mutation in common cold-causing HCoV-HKU1. In the SARS-CoV S structure, LA stabilizes the locked conformation, while the open, infectious conformation is devoid of LA. Electron tomography of SARS-CoV-2-infected cells reveals that LA treatment inhibits viral replication, resulting in fewer deformed virions. Our results establish FFA binding as a hallmark of pathogenic β-CoV infection and replication, setting the stage for FFA-based antiviral strategies to overcome COVID-19.
External linksSci Adv / PubMed:36417532 / PubMed Central
MethodsEM (single particle)
Resolution2.48 - 3.3 Å
Structure data

14717

7zh1

EMDB-14717, PDB-7zh1:
SARS CoV Spike protein, Closed C3 conformation
Method: EM (single particle) / Resolution: 2.48 Å

14718

7zh2

EMDB-14718, PDB-7zh2:
SARS CoV Spike protein, Closed C1 conformation
Method: EM (single particle) / Resolution: 2.71 Å

14724

7zh5

EMDB-14724, PDB-7zh5:
SARS CoV Spike protein, Open conformation
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-EIC:
LINOLEIC ACID / Linoleic acid

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • severe acute respiratory syndrome-related coronavirus
  • enterobacteria phage t4 (virus)
  • tequatrovirus t4
KeywordsVIRAL PROTEIN / SARS-CoV / Spike

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